OSGEP_XENLA
ID OSGEP_XENLA Reviewed; 335 AA.
AC Q7SYR1;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_03180};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase;
DE Short=t(6)A synthase;
DE AltName: Full=O-sialoglycoprotein endopeptidase {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein osgep {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein osgep {ECO:0000255|HAMAP-Rule:MF_03180};
GN Name=osgep {ECO:0000255|HAMAP-Rule:MF_03180};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Osgep likely
CC plays a direct catalytic role in this reaction, but requires other
CC protein(s) of the complex to fulfill this activity. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03180};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least
CC tp53rk, tprkb, osgep and lage3; the whole complex dimerizes.
CC {ECO:0000255|HAMAP-Rule:MF_03180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03180}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
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DR EMBL; BC054300; AAH54300.1; -; mRNA.
DR RefSeq; NP_001080787.1; NM_001087318.2.
DR RefSeq; XP_018081317.1; XM_018225828.1.
DR AlphaFoldDB; Q7SYR1; -.
DR SMR; Q7SYR1; -.
DR DNASU; 380480; -.
DR GeneID; 380480; -.
DR KEGG; xla:380480; -.
DR CTD; 380480; -.
DR Xenbase; XB-GENE-942951; osgep.L.
DR OrthoDB; 829465at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 380480; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000408; C:EKC/KEOPS complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; ISS:UniProtKB.
DR HAMAP; MF_01446; Kae1; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..335
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000096987"
FT BINDING 109
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 113
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 130..134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
SQ SEQUENCE 335 AA; 36936 MW; C8860F3FB17A1659 CRC64;
MTIVVGFEGS ANKIGVGIIQ DGKVLSNPRR TYITPPGQGF MPSDTARHHR SCILDVLQEA
LEESNIKPED VDCVAYTKGP GMGAPLLSVA IVARTVAQLW KKPLLGVNHC IGHIEMGRLI
TGAENPTVLY VSGGNTQVIA YSERCYRIFG ETIDIAVGNC LDRFARVLKI SNDPSPGYNI
EQMAKKGKKF VELPYTVKGM DVSFSGILSY IEDMSHKMLS SGECTPEDLC FSLQETLFSM
LVEITERAMA HCGSQEVLIV GGVGCNVRLQ EMMGVMCEER GAKIFATDER FCIDNGAMIA
QAGWEMFRAG QVTNLQDSWI TQRYRTDEVE VTWRD
